Literature DB >> 6197212

Determination of pancreatic carboxypeptidase A in human blood serum.

M Roth, A Rohner.   

Abstract

A method has been designed for the assay of pancreatic carboxypeptidase A in blood serum. It uses Z-Gly-Phe as the substrate and fluorimetric determination of the released phenylalanine in an amino acid analyser, which yields a measure of free carboxypeptidase A. In addition, the sum (free carboxypeptidase A + procarboxypeptidase A) can be determined on a second portion preincubated with trypsin, which converts the proenzyme to the active form. Determinations made in fifteen healthy individuals showed the presence of a measurable concentration of free carboxypeptidase A. In acute pancreatitis, total carboxypeptidase A is raised. An increase in circulating proenzyme is observed in some cases. Data from 46 patients show a good correlation between total carboxypeptidase A, lipase and immunoreactive trypsin. Differential determination of procarboxypeptidase A and free carboxypeptidase A provides an interesting new tool for the diagnosis of pancreatic disorders.

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Year:  1983        PMID: 6197212     DOI: 10.1016/0009-8981(83)90389-3

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  2 in total

1.  Evaluation of pro-carboxypeptidase A and carboxypeptidase A as serologic markers for adenocarcinoma of the pancreas.

Authors:  Peter Shamamian; Judith D Goldberg; Xiang Y Ye; Jonathan D Stewart; Peter J White; Charles Gilvarg
Journal:  HPB (Oxford)       Date:  2006       Impact factor: 3.647

2.  An intact C-terminal end of albumin is required for its long half-life in humans.

Authors:  Jeannette Nilsen; Esben Trabjerg; Algirdas Grevys; Claudia Azevedo; Stephen O Brennan; Maria Stensland; John Wilson; Kine Marita Knudsen Sand; Malin Bern; Bjørn Dalhus; Derry C Roopenian; Inger Sandlie; Kasper Dyrberg Rand; Jan Terje Andersen
Journal:  Commun Biol       Date:  2020-04-20
  2 in total

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